Skip to main content
NCBI home page
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1988 Nov;54(11):2808–2811. doi: 10.1128/aem.54.11.2808-2811.1988

Properties of the Cell Walls of Lactococcus lactis subsp. cremoris SK110 and SK112 and Their Relation to Bacteriophage Resistance

Lolke Sijtsma 1,*, Aart Sterkenburg 1,†, Jan T M Wouters 1,‡
PMCID: PMC204377  PMID: 16347779

Abstract

Resistance of Lactococcus lactis subsp. cremoris SK110 to bacteriophage sk11G, encoded on the plasmid pSK112, is due to poor phage adsorption. Its phage-sensitive variant SK112, cured of pSK112, adsorbs phages effectively. Incubation of SK112 with concanavalin A remarkably reduced phage adsorption to this strain. This treatment also caused agglutination of SK112 that was not found with SK110, indicating different concanavalin A adsorption characteristics of cell walls of both strains. The differences between the two strains were reduced by a mild alkali treatment of cells. This resulted in a positive agglutination with concanavalin A for both strains and in parallel adsorption of phage sk11G to both. Moreover, isolated cell walls of the two strains were investigated, and both bound phage sk11G. These observations suggest the presence of phage receptor material in SK112 as well as in SK110. SK110 contained a relatively high level of bound galactose when compared with the phage-sensitive SK112. After the mild alkali treatment, however, the galactose content of SK110 was diminished such that it became comparable with that of SK112. It is hypothesized that the alkali treatment liberates a galactose-containing component from the cell wall and causes phage sensitivity in L. lactis subsp. cremoris SK110.

Full text

PDF
2808

Images in this article

2809Image
on p.2809

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Archibald A. R., Coapes H. E. Blocking of bacteriophage receptor sites by Concanavalin A. J Gen Microbiol. 1972 Dec;73(3):581–585. doi: 10.1099/00221287-73-3-581. [DOI] [PubMed] [Google Scholar]
  2. GOLDSTEIN I. J., HOLLERMAN C. E., SMITH E. E. PROTEIN-CARBOHYDRATE INTERACTION. II. INHIBITION STUDIES ON THE INTERACTION OF CONCANAVALIN A WITH POLYSACCHARIDES. Biochemistry. 1965 May;4:876–883. doi: 10.1021/bi00881a013. [DOI] [PubMed] [Google Scholar]
  3. Glaser L., Ionesco H., Schaeffer P. Teichoic acids as components of a specific phage receptor in Bacillus subtilis. Biochim Biophys Acta. 1966 Aug 24;124(2):415–417. doi: 10.1016/0304-4165(66)90211-x. [DOI] [PubMed] [Google Scholar]
  4. Handelsman J., Ugalde R. A., Brill W. J. Rhizobium meliloti competitiveness and the alfalfa agglutinin. J Bacteriol. 1984 Mar;157(3):703–707. doi: 10.1128/jb.157.3.703-707.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hugenholtz J., Veldkamp H., Konings W. N. Detection of Specific Strains and Variants of Streptococcus cremoris in Mixed Cultures by Immunofluorescence. Appl Environ Microbiol. 1987 Jan;53(1):149–155. doi: 10.1128/aem.53.1.149-155.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kennedy A. F., Sutherland I. W. Analysis of bacterial exopolysaccharides. Biotechnol Appl Biochem. 1987 Feb;9(1):12–19. [PubMed] [Google Scholar]
  7. Keogh B. P., Pettingill G. Adsorption of Bacteriophage eb7 on Streptococcus cremoris EB7. Appl Environ Microbiol. 1983 Jun;45(6):1946–1948. doi: 10.1128/aem.45.6.1946-1948.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. King W. R., Collins E. B., Barrett E. L. Frequencies of Bacteriophage-Resistant and Slow Acid-Producing Variants of Streptococcus cremoris. Appl Environ Microbiol. 1983 May;45(5):1481–1485. doi: 10.1128/aem.45.5.1481-1485.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. MORSE S. I. Studies on the interactions between components of Staphylococcus aureus and Staphylococcus bacteriophage. J Exp Med. 1962 Aug 1;116:247–251. doi: 10.1084/jem.116.2.247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Nordström K., Forsgren A. Effect of protein A on adsorption of bacteriophages to Staphylococcus aureus. J Virol. 1974 Aug;14(2):198–202. doi: 10.1128/jvi.14.2.198-202.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Oram J. D. Isolation and properties of a phage receptor substance from the plasma membrane of Streptococcus lactis ML 3. J Gen Virol. 1971 Oct;13(1):59–71. doi: 10.1099/0022-1317-13-1-59. [DOI] [PubMed] [Google Scholar]
  12. Sanders M. E., Klaenhammer T. R. Characterization of Phage-Sensitive Mutants from a Phage-Insensitive Strain of Streptococcus lactis: Evidence for a Plasmid Determinant that Prevents Phage Adsorption. Appl Environ Microbiol. 1983 Nov;46(5):1125–1133. doi: 10.1128/aem.46.5.1125-1133.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Sanders M. E., Klaenhammer T. R. Phage Resistance in a Phage-Insensitive Strain of Streptococcus lactis: Temperature-Dependent Phage Development and Host-Controlled Phage Replication. Appl Environ Microbiol. 1984 May;47(5):979–985. doi: 10.1128/aem.47.5.979-985.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Sleytr U. B., Messner P. Crystalline surface layers on bacteria. Annu Rev Microbiol. 1983;37:311–339. doi: 10.1146/annurev.mi.37.100183.001523. [DOI] [PubMed] [Google Scholar]
  15. Terzaghi B. E., Sandine W. E. Improved medium for lactic streptococci and their bacteriophages. Appl Microbiol. 1975 Jun;29(6):807–813. doi: 10.1128/am.29.6.807-813.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Ugalde R. A., Coira J. A., Brill W. J. Biosynthesis of a galactose-and galacturonic acid-containing polysaccharide in Rhizobium meliloti. J Bacteriol. 1986 Oct;168(1):270–275. doi: 10.1128/jb.168.1.270-275.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Ugalde R. A., Handelsman J., Brill W. J. Role of galactosyltransferase activity in phage sensitivity and nodulation competitiveness of Rhizobium meliloti. J Bacteriol. 1986 Apr;166(1):148–154. doi: 10.1128/jb.166.1.148-154.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Vidaver A. K., Brock T. D. Purification and properties of a bacteriophage receptor material from Streptococcus faecium. Biochim Biophys Acta. 1966 Jun 29;121(2):298–314. doi: 10.1016/0304-4165(66)90119-x. [DOI] [PubMed] [Google Scholar]
  19. Wallace R. J. Cytoplasmic reserve polysaccharide of Selenomonas ruminantium. Appl Environ Microbiol. 1980 Mar;39(3):630–634. doi: 10.1128/aem.39.3.630-634.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Wu T. C., Park J. T. Chemical characterization of a new surface antigenic polysaccharide from a mutant of Staphylococcus aureus. J Bacteriol. 1971 Nov;108(2):874–884. doi: 10.1128/jb.108.2.874-884.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Yokokura T. Phage receptor material in Lactobacillus casei cell wall. I. Effect of L-rhamnose on phage adsorption to the cell wall. Jpn J Microbiol. 1971 Sep;15(5):457–463. doi: 10.1111/j.1348-0421.1971.tb00604.x. [DOI] [PubMed] [Google Scholar]
  22. Yokokura T. Phage receptor material in Lactobacillus casei. J Gen Microbiol. 1977 May;100(1):139–145. doi: 10.1099/00221287-100-1-139. [DOI] [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES